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Database: PDB
Entry: 4OK1
LinkDB: 4OK1
Original site: 4OK1 
HEADER    HORMONE RECEPTOR/PEPTIDE                21-JAN-14   4OK1              
TITLE     CRYSTAL STRUCTURE OF W741L-AR-LBD BOUND WITH CO-REGULATOR PEPTIDE     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ANDROGEN RECEPTOR;                                         
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: LIGAND BINDING DOAMIN;                                     
COMPND   5 SYNONYM: DIHYDROTESTOSTERONE RECEPTOR, NUCLEAR RECEPTOR SUBFAMILY 3  
COMPND   6 GROUP C MEMBER 4;                                                    
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MUTATION: YES;                                                       
COMPND   9 MOL_ID: 2;                                                           
COMPND  10 MOLECULE: CO-REGULATOR PEPTIDE;                                      
COMPND  11 CHAIN: B;                                                            
COMPND  12 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: AR, DHTR, NR3C4;                                               
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PET28;                                    
SOURCE  10 MOL_ID: 2;                                                           
SOURCE  11 SYNTHETIC: YES                                                       
KEYWDS    ALPHA-HELIX, HORMONE/GROWTH FACTOR RECEPTOR, PHOSPHORYLATION, HORMONE 
KEYWDS   2 RECEPTOR-PEPTIDE COMPLEX, SIGNAL TRANSDUCTION                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.S.LIU,C.L.HSU,W.G.WU                                                
REVDAT   2   24-DEC-14 4OK1    1       JRNL                                     
REVDAT   1   20-AUG-14 4OK1    0                                                
JRNL        AUTH   C.L.HSU,J.S.LIU,P.L.WU,H.H.GUAN,Y.L.CHEN,A.C.LIN,H.J.TING,   
JRNL        AUTH 2 S.T.PANG,S.D.YEH,W.L.MA,C.J.CHEN,W.G.WU,C.CHANG              
JRNL        TITL   IDENTIFICATION OF A NEW ANDROGEN RECEPTOR (AR) CO-REGULATOR  
JRNL        TITL 2 BUD31 AND RELATED PEPTIDES TO SUPPRESS WILD-TYPE AND MUTATED 
JRNL        TITL 3 AR-MEDIATED PROSTATE CANCER GROWTH VIA PEPTIDE SCREENING AND 
JRNL        TITL 4 X-RAY STRUCTURE ANALYSIS.                                    
JRNL        REF    MOL ONCOL                     V.   8  1575 2014              
JRNL        REFN                                                                
JRNL        PMID   25091737                                                     
JRNL        DOI    10.1016/J.MOLONC.2014.06.009                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.09 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.7.0029                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.09                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 13901                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.197                           
REMARK   3   R VALUE            (WORKING SET) : 0.195                           
REMARK   3   FREE R VALUE                     : 0.249                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 738                             
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.09                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.14                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 812                          
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 77.25                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3380                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 37                           
REMARK   3   BIN FREE R VALUE                    : 0.3300                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2096                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 29                                      
REMARK   3   SOLVENT ATOMS            : 36                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 52.71                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.87000                                             
REMARK   3    B22 (A**2) : 0.37000                                              
REMARK   3    B33 (A**2) : 0.50000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : -0.00000                                             
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.274         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.212         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.190         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 7.530         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.965                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.947                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2189 ; 0.015 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  2959 ; 1.806 ; 1.970       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   257 ; 6.073 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   102 ;32.739 ;23.627       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   392 ;17.940 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    14 ;15.818 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   322 ; 0.123 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1638 ; 0.009 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN USED IF PRESENT IN    
REMARK   3  THE INPUT                                                           
REMARK   4                                                                      
REMARK   4 4OK1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-JAN-14.                  
REMARK 100 THE RCSB ID CODE IS RCSB084590.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 150                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : NSRRC                              
REMARK 200  BEAMLINE                       : BL13B1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0                                
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 14685                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.090                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 28.100                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.6                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : 0.07000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.09                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.16                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 81.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.37900                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 4.160                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: PDB ENTRY 4OJB                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 39.96                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.05                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.6M MAGNESIUM SULPHATE, 0.1M MES, PH    
REMARK 280  6.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       26.72550            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       34.82950            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       33.04300            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       34.82950            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       26.72550            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       33.04300            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1710 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 11980 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -9.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLN A   919                                                      
REMARK 465     ARG B     0                                                      
REMARK 465     VAL B    10                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    VAL A 730      -35.69    -36.15                                   
REMARK 500    VAL A 757       22.77   -146.78                                   
REMARK 500    ASN A 823       72.83   -114.40                                   
REMARK 500    LYS A 847       18.20    -66.76                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 198 A 1001                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4OEA   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4OED   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4OEY   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4OEZ   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4OFR   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4OFU   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4OGH   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4OH5   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4OH6   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4OHA   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4OIL   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4OIU   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4OJ9   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4OJB   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4OKB   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4OKT   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4OKW   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4OKX   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4OLM   RELATED DB: PDB                                   
DBREF  4OK1 A  670   919  UNP    P10275   ANDR_HUMAN     670    919             
DBREF  4OK1 B    0    10  PDB    4OK1     4OK1             0     10             
SEQADV 4OK1 LEU A  741  UNP  P10275    TRP   741 ENGINEERED MUTATION            
SEQADV 4OK1 ALA A  760  UNP  P10275    ARG   760 ENGINEERED MUTATION            
SEQRES   1 A  250  GLN PRO ILE PHE LEU ASN VAL LEU GLU ALA ILE GLU PRO          
SEQRES   2 A  250  GLY VAL VAL CYS ALA GLY HIS ASP ASN ASN GLN PRO ASP          
SEQRES   3 A  250  SER PHE ALA ALA LEU LEU SER SER LEU ASN GLU LEU GLY          
SEQRES   4 A  250  GLU ARG GLN LEU VAL HIS VAL VAL LYS TRP ALA LYS ALA          
SEQRES   5 A  250  LEU PRO GLY PHE ARG ASN LEU HIS VAL ASP ASP GLN MET          
SEQRES   6 A  250  ALA VAL ILE GLN TYR SER LEU MET GLY LEU MET VAL PHE          
SEQRES   7 A  250  ALA MET GLY TRP ARG SER PHE THR ASN VAL ASN SER ALA          
SEQRES   8 A  250  MET LEU TYR PHE ALA PRO ASP LEU VAL PHE ASN GLU TYR          
SEQRES   9 A  250  ARG MET HIS LYS SER ARG MET TYR SER GLN CYS VAL ARG          
SEQRES  10 A  250  MET ARG HIS LEU SER GLN GLU PHE GLY TRP LEU GLN ILE          
SEQRES  11 A  250  THR PRO GLN GLU PHE LEU CYS MET LYS ALA LEU LEU LEU          
SEQRES  12 A  250  PHE SER ILE ILE PRO VAL ASP GLY LEU LYS ASN GLN LYS          
SEQRES  13 A  250  PHE PHE ASP GLU LEU ARG MET ASN TYR ILE LYS GLU LEU          
SEQRES  14 A  250  ASP ARG ILE ILE ALA CYS LYS ARG LYS ASN PRO THR SER          
SEQRES  15 A  250  CYS SER ARG ARG PHE TYR GLN LEU THR LYS LEU LEU ASP          
SEQRES  16 A  250  SER VAL GLN PRO ILE ALA ARG GLU LEU HIS GLN PHE THR          
SEQRES  17 A  250  PHE ASP LEU LEU ILE LYS SER HIS MET VAL SER VAL ASP          
SEQRES  18 A  250  PHE PRO GLU MET MET ALA GLU ILE ILE SER VAL GLN VAL          
SEQRES  19 A  250  PRO LYS ILE LEU SER GLY LYS VAL LYS PRO ILE TYR PHE          
SEQRES  20 A  250  HIS THR GLN                                                  
SEQRES   1 B   11  ARG GLY ALA PHE GLN ASN LEU PHE GLN SER VAL                  
HET    198  A1001      29                                                       
HETNAM     198 R-BICALUTAMIDE                                                   
HETSYN     198 (2R)-N-[4-CYANO-3-(TRIFLUOROMETHYL)PHENYL]-3-[(4-                
HETSYN   2 198  FLUOROPHENYL)SULFONYL]-2-HYDROXY-2-METHYLPROPANAMIDE            
FORMUL   3  198    C18 H14 F4 N2 O4 S                                           
FORMUL   4  HOH   *36(H2 O)                                                     
HELIX    1   1 PRO A  671  GLU A  681  1                                  11    
HELIX    2   2 SER A  696  ALA A  721  1                                  26    
HELIX    3   3 GLY A  724  LEU A  728  5                                   5    
HELIX    4   4 HIS A  729  ASN A  758  1                                  30    
HELIX    5   5 ASN A  771  SER A  778  1                                   8    
HELIX    6   6 MET A  780  LEU A  797  1                                  18    
HELIX    7   7 THR A  800  PHE A  813  1                                  14    
HELIX    8   8 ASN A  823  ILE A  842  1                                  20    
HELIX    9   9 ASN A  848  LYS A  883  1                                  36    
HELIX   10  10 SER A  884  SER A  888  5                                   5    
HELIX   11  11 PRO A  892  GLN A  902  1                                  11    
HELIX   12  12 GLN A  902  SER A  908  1                                   7    
HELIX   13  13 ALA B    2  SER B    9  1                                   8    
SHEET    1   A 2 LEU A 762  ALA A 765  0                                        
SHEET    2   A 2 LEU A 768  PHE A 770 -1  O  PHE A 770   N  LEU A 762           
SHEET    1   B 2 ILE A 815  PRO A 817  0                                        
SHEET    2   B 2 VAL A 911  PRO A 913 -1  O  LYS A 912   N  ILE A 816           
SSBOND   1 CYS A  844    CYS A  852                          1555   1555  2.04  
SITE     1 AC1 15 LEU A 704  ASN A 705  LEU A 707  GLY A 708                    
SITE     2 AC1 15 GLN A 711  MET A 742  MET A 745  VAL A 746                    
SITE     3 AC1 15 MET A 749  ARG A 752  PHE A 764  MET A 787                    
SITE     4 AC1 15 LEU A 873  MET A 895  ILE A 899                               
CRYST1   53.451   66.086   69.659  90.00  90.00  90.00 P 21 21 21    4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.018709  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.015132  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.014356        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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